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Conserved domains on  [gi|971825946|ref|NP_001305311|]
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inversin isoform d [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-234 5.75e-53

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.16  E-value: 5.75e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   1 MWAAGKGSDDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVI 80
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  81 QTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQD 160
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971825946 161 KEGRTALHWSCNNGYLDAIKLLLDFAAFPNqmENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAF 234
Cdd:COG0666  217 NDGKTALDLAAENGNLEIVKLLLEAGADLN--AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 292-506 1.92e-05

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.24  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  292 CRPQALPCLPSTQDVPSRQSRAPSKQPPAGNVAQGPEP---RDSRGSPGGSLGGALQKEQHVSSDLQGTNSRRPNET--- 365
Cdd:PHA03307  185 APSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPapgRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPApit 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  366 ------AREHSKGQSACVHFRPNEGSDGSRHPgVPSVEKSRGETAGDERCAKGKGFVKQPSCIrvAGPDEKGEDSRRAAA 439
Cdd:PHA03307  265 lptriwEASGWNGPSSRPGPASSSSSPRERSP-SPSPSSPGSGPAPSSPRASSSSSSSRESSS--SSTSSSSESSRGAAV 341

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971825946  440 SL-PPHDSHWKPSRrhdTEPKAKCAPQKRRTQELRGGRCSPAGSSRPGSARGEAVHAGQNPPHHRTPR 506
Cdd:PHA03307  342 SPgPSPSRSPSPSR---PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGR 406
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 583-614 3.28e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


:

Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 38.68  E-value: 3.28e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 971825946 583 RKELFRKKNKAAAVIQRAWRSYQLRKHLSHLR 614
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 227-253 1.82e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


:

Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 36.37  E-value: 1.82e-03
                         10        20
                 ....*....|....*....|....*..
gi 971825946 227 AIQDIAAFKIQAVYKGYKVRKAFRDRK 253
Cdd:cd23767    6 QRMNRAATLIQALWRGYKVRKELKKKK 32
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-234 5.75e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.16  E-value: 5.75e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   1 MWAAGKGSDDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVI 80
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  81 QTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQD 160
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971825946 161 KEGRTALHWSCNNGYLDAIKLLLDFAAFPNqmENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAF 234
Cdd:COG0666  217 NDGKTALDLAAENGNLEIVKLLLEAGADLN--AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 10-228 5.80e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 105.13  E-value: 5.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  10 DVLRTMLslKSDIDINMADKYGGTALHAAALSGHVST-----VKLLLENNAQVDATDVMKHTPLFRA--CEMGHKDVIQT 82
Cdd:PHA03100  49 DVVKILL--DNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEY 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  83 LIKGGARVDLVDQDGHSLLHWAALGGNAD--VCQILIENKINPNVQDYagrtplqcaayggyINCmavLMENNADPNIQD 160
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR--------------VNY---LLSYGVPINIKD 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971825946 161 KEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEerYTPLDYALLGERHEVIQFMLEHGAlSIAAI 228
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG--DTPLHIAILNNNKEIFKLLLNNGP-SIKTI 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
68-160 2.86e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 2.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   68 LFRACEMGHKDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIEnKINPNVQDYaGRTPLQCAAYGGYINCMA 147
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 971825946  148 VLMENNADPNIQD 160
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 24-171 1.63e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  24 INMA---DKYGG-TALHAAALSGHVSTVKLLLENNAQV---DATDVM------------KHTPLFRACeMGHKDVIQTLI 84
Cdd:cd22192   78 VNEPmtsDLYQGeTALHIAVVNQNLNLVRELIARGADVvspRATGTFfrpgpknliyygEHPLSFAAC-VGNEEIVRLLI 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  85 KGGArvDLVDQD--GHSLLHWAALGGNAD-VCQI--LI---ENKINP----NVQDYAGRTPLQCAAYGGYINCMAVLMEN 152
Cdd:cd22192  157 EHGA--DIRAQDslGNTVLHILVLQPNKTfACQMydLIlsyDKEDDLqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234

                        170
                 ....*....|....*....
gi 971825946 153 nadpniqdkegRTALHWSC 171
Cdd:cd22192  235 -----------RRHIQWTY 242
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 292-506 1.92e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.24  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  292 CRPQALPCLPSTQDVPSRQSRAPSKQPPAGNVAQGPEP---RDSRGSPGGSLGGALQKEQHVSSDLQGTNSRRPNET--- 365
Cdd:PHA03307  185 APSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPapgRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPApit 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  366 ------AREHSKGQSACVHFRPNEGSDGSRHPgVPSVEKSRGETAGDERCAKGKGFVKQPSCIrvAGPDEKGEDSRRAAA 439
Cdd:PHA03307  265 lptriwEASGWNGPSSRPGPASSSSSPRERSP-SPSPSSPGSGPAPSSPRASSSSSSSRESSS--SSTSSSSESSRGAAV 341

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971825946  440 SL-PPHDSHWKPSRrhdTEPKAKCAPQKRRTQELRGGRCSPAGSSRPGSARGEAVHAGQNPPHHRTPR 506
Cdd:PHA03307  342 SPgPSPSRSPSPSR---PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGR 406
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 96-125 2.50e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 2.50e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 971825946    96 DGHSLLHWAALGGNADVCQILIENKINPNV 125
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 583-614 3.28e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 38.68  E-value: 3.28e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 971825946 583 RKELFRKKNKAAAVIQRAWRSYQLRKHLSHLR 614
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-219 6.89e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.15  E-value: 6.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946    3 AAGKGSDDVLRTMLSLKSDIDINMADKYGGTALHAAALSG-HVSTVKLLLENNAQVDATDVMKHT---PLFRACEMGHKD 78
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAislEYVDAVEAILLH 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   79 VIQTLIKGGARVDLVDQD------GHSLLHWAALGGNADVCQILIENKINPNV------------QDYA--GRTPLQCAA 138
Cdd:TIGR00870 104 LLAAFRKSGPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  139 YGGYINCMAVLMENNADPNIQDKEGRTALH-------WSCNNGYL-----DAIKLLLDFAAFPNQMEN--NEERYTPLDY 204
Cdd:TIGR00870 184 CLGSPSIVALLSEDPADILTADSLGNTLLHllvmeneFKAEYEELscqmyNFALSLLDKLRDSKELEVilNHQGLTPLKL 263

                         250
                  ....*....|....*
gi 971825946  205 ALLGERHEVIQFMLE 219
Cdd:TIGR00870 264 AAKEGRIVLFRLKLA 278
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 227-253 1.82e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 36.37  E-value: 1.82e-03
                         10        20
                 ....*....|....*....|....*..
gi 971825946 227 AIQDIAAFKIQAVYKGYKVRKAFRDRK 253
Cdd:cd23767    6 QRMNRAATLIQALWRGYKVRKELKKKK 32
COG3416 COG3416
Uncharacterized conserved protein, DUF2076 domain [Function unknown];
260-345 7.20e-03

Uncharacterized conserved protein, DUF2076 domain [Function unknown];


Pssm-ID: 442642 [Multi-domain]  Cd Length: 237  Bit Score: 38.85  E-value: 7.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 260 EQLRKDAAAKKREEENKRKEAEQQKGRRSP----------DSCRPQALPCLPSTQDVPSRQS----RAPSKQPPAGNVAQ 325
Cdd:COG3416   54 EAALKQAQQRIQELEAQLAQLQQQQPQSSGgflsglfgggQRPPPAPQPSQPGPQQQPAPPSgpwgQAAPQQPGYGQPQY 133

                         90       100
                 ....*....|....*....|.
gi 971825946 326 G-PEPRDSRGspGGSLGGALQ 345
Cdd:COG3416  134 GqPAAGPSGG--GGFLGGALQ 152
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-234 5.75e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.16  E-value: 5.75e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   1 MWAAGKGSDDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVI 80
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  81 QTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQD 160
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971825946 161 KEGRTALHWSCNNGYLDAIKLLLDFAAFPNqmENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAF 234
Cdd:COG0666  217 NDGKTALDLAAENGNLEIVKLLLEAGADLN--AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-268 3.24e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.15  E-value: 3.24e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   9 DDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKGGA 88
Cdd:COG0666   32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  89 RVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALH 168
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 169 WSCNNGYLDAIKLLLDFAAFPNQMenNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAFKIQAVYKGYKVRKA 248
Cdd:COG0666  192 LAAENGHLEIVKLLLEAGADVNAK--DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                        250       260
                 ....*....|....*....|
gi 971825946 249 FRDRKNLLMKHEQLRKDAAA 268
Cdd:COG0666  270 LLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-287 6.43e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.12  E-value: 6.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  16 LSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKGGARVDLVDQ 95
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  96 DGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGY 175
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 176 LDAIKLLLDFAAFPNQMENNEEryTPLDYALLGERHEVIQFMLEHGA------------LSIAAIQDIAAFKIQAVYKGY 243
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGE--TPLHLAAENGHLEIVKLLLEAGAdvnakdndgktaLDLAAENGNLEIVKLLLEAGA 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 971825946 244 KVRKAFRDRKNLLMKHEQLRKDAAAKKREEENKRKEAEQQKGRR 287
Cdd:COG0666  244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-222 4.02e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 4.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  47 VKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQ 126
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 127 DYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMenNEERYTPLDYAL 206
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ--DNDGNTPLHLAA 161

                        170
                 ....*....|....*.
gi 971825946 207 LGERHEVIQFMLEHGA 222
Cdd:COG0666  162 ANGNLEIVKLLLEAGA 177
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 10-228 5.80e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 105.13  E-value: 5.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  10 DVLRTMLslKSDIDINMADKYGGTALHAAALSGHVST-----VKLLLENNAQVDATDVMKHTPLFRA--CEMGHKDVIQT 82
Cdd:PHA03100  49 DVVKILL--DNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEY 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  83 LIKGGARVDLVDQDGHSLLHWAALGGNAD--VCQILIENKINPNVQDYagrtplqcaayggyINCmavLMENNADPNIQD 160
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR--------------VNY---LLSYGVPINIKD 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971825946 161 KEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEerYTPLDYALLGERHEVIQFMLEHGAlSIAAI 228
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG--DTPLHIAILNNNKEIFKLLLNNGP-SIKTI 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
68-160 2.86e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 2.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   68 LFRACEMGHKDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIEnKINPNVQDYaGRTPLQCAAYGGYINCMA 147
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 971825946  148 VLMENNADPNIQD 160
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-192 3.09e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 3.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  101 LHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMEnNADPNIQDkEGRTALHWSCNNGYLDAIK 180
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 971825946  181 LLLDFAAFPNQM 192
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
35-127 5.07e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 5.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   35 LHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKgGARVDLVDqDGHSLLHWAALGGNADVCQ 114
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 971825946  115 ILIENKINPNVQD 127
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
134-222 1.35e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  134 LQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFpnqmENNEERYTPLDYALLGERHEV 213
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLEI 76


                  ....*....
gi 971825946  214 IQFMLEHGA 222
Cdd:pfam12796  77 VKLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-94 5.65e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 5.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946    1 MWAAGKGSDDVLRTMLslKSDIDINMADKYGGTALHAAALSGHVSTVKLLLEnNAQVDATDvMKHTPLFRACEMGHKDVI 80
Cdd:pfam12796   2 HLAAKNGNLELVKLLL--ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 971825946   81 QTLIKGGARVDLVD 94
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 8-240 1.86e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 86.66  E-value: 1.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   8 SDDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVST-VKLLLENNAQVDATDVMKHTPLFRACEMGH-KDVIQTLIK 85
Cdd:PHA02876 250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIM 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  86 GGARVDLVDQDGHSLLHWAA-LGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGR 164
Cdd:PHA02876 330 LGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG 409

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971825946 165 TALHWS-CNNGYLDAIKLLLDFAAfpNQMENNEERYTPLDYALLGE-RHEVIQFMLEHGAlsiaaiqDIAAFKIQAVY 240
Cdd:PHA02876 410 TALHFAlCGTNPYMSVKTLIDRGA--NVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGA-------DVNAINIQNQY 478
PHA03095 PHA03095
ankyrin-like protein; Provisional
 10-169 3.06e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.08  E-value: 3.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  10 DVLRTMLSLKSDIdiNMADKYGGTALHAAaLSG---HVSTVKLLLENNAQVDATDVMKHTPL-----FRACEMghkDVIQ 81
Cdd:PHA03095  98 DVIKLLIKAGADV--NAKDKVGRTPLHVY-LSGfniNPKVIRLLLRKGADVNALDLYGMTPLavllkSRNANV---ELLR 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  82 TLIKGGARVDLVDQDGHSLLHWAALG--GNADVCQILIENKINPNVQDYAGRTPLQCAAYGGyiNCMAVLM----ENNAD 155
Cdd:PHA03095 172 LLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS--SCKRSLVlpllIAGIS 249

                        170
                 ....*....|....
gi 971825946 156 PNIQDKEGRTALHW 169
Cdd:PHA03095 250 INARNRYGQTPLHY 263
PHA03095 PHA03095
ankyrin-like protein; Provisional
 18-222 6.35e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.22  E-value: 6.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  18 LKSDIDINMADKYGGTALHAAALSGH---VSTVKLLLENNAQVDATDVMKHTPLFraCEMGHK---DVIQTLIKGGARVD 91
Cdd:PHA03095  34 LAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLH--LYLYNAttlDVIKLLIKAGADVN 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  92 LVDQDGHSLLHwAALGG---NADVCQILIENKINPNVQDYAGRTPLqcAAYGGYINC----MAVLMENNADPNIQDKEGR 164
Cdd:PHA03095 112 AKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNAnvelLRLLIDAGADVYAVDDRFR 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 165 TALHWSCNNGYLDAIKLLLDFAAFPNQMENNEERYTPLDYALLGE--RHEVIQFMLEHGA 222
Cdd:PHA03095 189 SLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGI 248
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 9-206 1.10e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.93  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   9 DDVLRTMLslKSDIDINMADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKGGA 88
Cdd:PHA02874 104 KDMIKTIL--DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  89 RVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYggYINCMAVLMENNADPNIQDKEGRTALH 168
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLH 259

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 971825946 169 WSCNNG-YLDAIKLLLDFAAFPNQMENNEEryTPLDYAL 206
Cdd:PHA02874 260 HAINPPcDIDIIDILLYHKADISIKDNKGE--NPIDTAF 296
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 24-231 1.42e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.54  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  24 INMADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMG-----------------------HKDVI 80
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGahdiikllidngvdtsilpipciEKDMI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  81 QTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQD 160
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971825946 161 KEGRTALHWSCNNGYLDAIKLLLDFAAfpNQMENNEERYTPLDYALLGERhEVIQFMLEHGALSiaaIQDI 231
Cdd:PHA02874 188 NNGESPLHNAAEYGDYACIKLLIDHGN--HIMNKCKNGFTPLHNAIIHNR-SAIELLINNASIN---DQDI 252
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 44-222 2.91e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.47  E-value: 2.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  44 VSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKGGARVDLVDQDGHSLLHWAA-----LGGNADVCQILIE 118
Cdd:PHA03100  15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 119 NKINPNVQDYAGRTPLQCAAYG--GYINCMAVLMENNADPNIQDKEGRTALHW--SCNNGYLDAIKLLLDFAAFPNQMEN 194
Cdd:PHA03100  95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLylESNKIDLKILKLLIDKGVDINAKNR 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 971825946 195 --------------NEERYTPLDYALLGERHEVIQFMLEHGA 222
Cdd:PHA03100 175 vnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGA 216
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 7-222 4.80e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.56  E-value: 4.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   7 GSDDVLRTMLSLKSDIDINMADKYggTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKG 86
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGI--SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  87 GARV-DLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRT 165
Cdd:PHA02875  91 GKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 971825946 166 ALHWSCNNGYLDAIKLLLDFAAFPNQMENNEErYTPLDYALLGERHEVIQFMLEHGA 222
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGC-VAALCYAIENNKIDIVRLFIKRGA 226
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 12-222 1.25e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.25  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  12 LRTMLSLKSDIdiNMADKYGGTALH-AAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKGGARV 90
Cdd:PHA02876 324 IRTLIMLGADV--NAADRLYITPLHqASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  91 DLVDQDGHSLLHWAALGGNAdvcqilienkinpnvqdyagrtplqcaayggYINcMAVLMENNADPNIQDKEGRTALHWS 170
Cdd:PHA02876 402 EALSQKIGTALHFALCGTNP-------------------------------YMS-VKTLIDRGANVNSKNKDLSTPLHYA 449

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 971825946 171 C-NNGYLDAIKLLLDFAAFPNQMeNNEERYtPLDYALlgERHEVIQFMLEHGA 222
Cdd:PHA02876 450 CkKNCKLDVIEMLLDNGADVNAI-NIQNQY-PLLIAL--EYHGIVNILLHYGA 498
Ank_4 pfam13637
Ankyrin repeats (many copies);
31-84 4.34e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 4.34e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 971825946   31 GGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLI 84
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 29-172 5.77e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 5.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  29 KYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKGGARVDLVDQDGHSLLHWAALGG 108
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971825946 109 NADVCQILIENKINPNvqdYAGRTP---LQCAAY-GGYINCMAVLMENNADPNIQ---DKEGRTALHWSCN 172
Cdd:PHA02875 180 DIAICKMLLDSGANID---YFGKNGcvaALCYAIeNNKIDIVRLFIKRGADCNIMfmiEGEECTILDMICN 247
PHA03095 PHA03095
ankyrin-like protein; Provisional
 78-269 8.74e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.05  E-value: 8.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  78 DVIQTLIKGGARVDLVDQDGHSLLHwaALGGN-----ADVCQILIENKINPNVQDYAGRTPLQCAAYGGY-INCMAVLME 151
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLH--LYLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 152 NNADPNIQDKEGRTALHWSCNNGYLDA--IKLLLDFAAFPNQMENNEerYTPLDyALLGERH---EVIQFMLEHGAlSIA 226
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVYLSGFNINPkvIRLLLRKGADVNALDLYG--MTPLA-VLLKSRNanvELLRLLIDAGA-DVY 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 971825946 227 AIQDI--AAFKIQAVYkgykvrkaFRDRKNLLMKHEQLRKDAAAK 269
Cdd:PHA03095 182 AVDDRfrSLLHHHLQS--------FKPRARIVRELIRAGCDPAAT 218
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 6-167 1.07e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.52  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   6 KGSDDVLRTM---LSLKSDIDINMADKYGG-TALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQ 81
Cdd:PHA02878 139 KSKDDIIEAEitkLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVH 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  82 TLIKGGARVDLVDQDGHSLLHWA-ALGGNADVCQILIENKINPNVQDYA-GRTPLQCAAYGGYIncMAVLMENNADPNIQ 159
Cdd:PHA02878 219 ILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSL 296


                 ....*...
gi 971825946 160 DKEGRTAL 167
Cdd:PHA02878 297 NSYKLTPL 304
PHA03095 PHA03095
ankyrin-like protein; Provisional
 44-184 1.08e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  44 VSTVKLLLENNAQVDATDVMKHTPLfraCEMGH------KDVIQTLIKGGARVDLVDQDGHSLLHWAALGGN-ADVCQIL 116
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPL---HLYLHyssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLL 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971825946 117 IENKINPNVQDYAGRTPLQCAAYGGYIN-CMA-VLMENNADPNIQDKEGRTALHW--SCNNGYLDAIKLLLD 184
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLHVYLSGFNINpKVIrLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLID 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
97-149 1.09e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 1.09e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 971825946   97 GHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVL 149
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
 78-203 1.28e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 64.47  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  78 DVIQTLIKGGARVDLVDQDGHS-----LLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVL--- 149
Cdd:PHA02798  52 DIVKLFINLGANVNGLDNEYSTplctiLSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlfm 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 971825946 150 MENNADPNIQDKEGRTALH---WSCNNGYLDAIKLLLDFAAFPNQMeNNEERYTPLD 203
Cdd:PHA02798 132 IENGADTTLLDKDGFTMLQvylQSNHHIDIEIIKLLLEKGVDINTH-NNKEKYDTLH 187
Ank_4 pfam13637
Ankyrin repeats (many copies);
130-183 3.45e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 3.45e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 971825946  130 GRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLL 183
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 9-232 2.54e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.46  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   9 DDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKGGA 88
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  89 RV---DL--------VDQDGHSLLHWAALGGNA-DVCQ------------------ILIENKINPNVQDYAGRTPLQCAA 138
Cdd:PHA02876 236 NInknDLsllkairnEDLETSLLLYDAGFSVNSiDDCKntplhhasqapslsrlvpKLLERGADVNAKNIKGETPLYLMA 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 139 YGGY-INCMAVLMENNADPNIQDKEGRTALHWSCN-NGYLDAIKLLLDFAAFPNQMENNEEryTPLDYALLGERHEVIQF 216
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDK--TPIHYAAVRNNVVIINT 393

                        250
                 ....*....|....*.
gi 971825946 217 MLEHGALSIAAIQDIA 232
Cdd:PHA02876 394 LLDYGADIEALSQKIG 409
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 18-95 2.84e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 2.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971825946  18 LKSDIDINMADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKGGARVDLVDQ 95
Cdd:PHA03100 179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 100-183 3.44e-09

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 3.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 100 LLHWAAlGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAI 179
Cdd:PTZ00322  86 LCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                 ....
gi 971825946 180 KLLL 183
Cdd:PTZ00322 165 QLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 3-155 3.52e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.27  E-value: 3.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   3 AAGKGSDDVLRTMLSLKSDIDInmADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQT 82
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDI--GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRI 609

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971825946  83 LIKGGARVDlvDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNAD 155
Cdd:PLN03192 610 LYHFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 148-220 4.31e-09

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 4.31e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971825946 148 VLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEEryTPLDYALLGERHEVIQFMLEH 220
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK--TPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
66-117 5.19e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 5.19e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 971825946   66 TPLFRACEMGHKDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILI 117
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
2-51 1.04e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 1.04e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 971825946    2 WAAGKGSDDVLRTMLSLKsdIDINMADKYGGTALHAAALSGHVSTVKLLL 51
Cdd:pfam13637   7 AAAASGHLELLRLLLEKG--ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 104-190 5.39e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 5.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 104 AALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLL 183
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611


                 ....*..
gi 971825946 184 DFAAFPN 190
Cdd:PLN03192 612 HFASISD 618
Ank_5 pfam13857
Ankyrin repeats (many copies);
116-168 1.87e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 1.87e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 971825946  116 LIENK-INPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALH 168
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 104-222 3.07e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 3.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 104 AALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLL 183
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 971825946 184 DFAAFPNQMeNNEERYTPLDYALLGERHEVIQFMLEHGA 222
Cdd:PHA02875  89 DLGKFADDV-FYKDGMTPLHLATILKKLDIMKLLIARGA 126
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 39-116 4.26e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 4.26e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971825946  39 ALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQIL 116
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 21-183 4.89e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  21 DIDINMAdkyggTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKGGARVDLVDQDGHSL 100
Cdd:PLN03192 520 HDDPNMA-----SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 101 LHWAALGGNADVCQILIE--NKINPnvqdYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDA 178
Cdd:PLN03192 595 LWNAISAKHHKIFRILYHfaSISDP----HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM 670


                 ....*
gi 971825946 179 IKLLL 183
Cdd:PLN03192 671 VRLLI 675
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 8-85 5.01e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 5.01e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971825946   8 SDDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIK 85
Cdd:PTZ00322  92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
153-205 6.70e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 6.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 971825946  153 NADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNqmENNEERYTPLDYA 205
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLN--LKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
86-137 1.04e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.04e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 971825946   86 GGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCA 137
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
163-218 1.28e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 971825946  163 GRTALHWSCNNGYLDAIKLLLDFAAFPNqmENNEERYTPLDYALLGERHEVIQFML 218
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN--AVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 24-171 1.63e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  24 INMA---DKYGG-TALHAAALSGHVSTVKLLLENNAQV---DATDVM------------KHTPLFRACeMGHKDVIQTLI 84
Cdd:cd22192   78 VNEPmtsDLYQGeTALHIAVVNQNLNLVRELIARGADVvspRATGTFfrpgpknliyygEHPLSFAAC-VGNEEIVRLLI 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  85 KGGArvDLVDQD--GHSLLHWAALGGNAD-VCQI--LI---ENKINP----NVQDYAGRTPLQCAAYGGYINCMAVLMEN 152
Cdd:cd22192  157 EHGA--DIRAQDslGNTVLHILVLQPNKTfACQMydLIlsyDKEDDLqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234

                        170
                 ....*....|....*....
gi 971825946 153 nadpniqdkegRTALHWSC 171
Cdd:cd22192  235 -----------RRHIQWTY 242
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 292-506 1.92e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.24  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  292 CRPQALPCLPSTQDVPSRQSRAPSKQPPAGNVAQGPEP---RDSRGSPGGSLGGALQKEQHVSSDLQGTNSRRPNET--- 365
Cdd:PHA03307  185 APSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPapgRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPApit 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  366 ------AREHSKGQSACVHFRPNEGSDGSRHPgVPSVEKSRGETAGDERCAKGKGFVKQPSCIrvAGPDEKGEDSRRAAA 439
Cdd:PHA03307  265 lptriwEASGWNGPSSRPGPASSSSSPRERSP-SPSPSSPGSGPAPSSPRASSSSSSSRESSS--SSTSSSSESSRGAAV 341

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971825946  440 SL-PPHDSHWKPSRrhdTEPKAKCAPQKRRTQELRGGRCSPAGSSRPGSARGEAVHAGQNPPHHRTPR 506
Cdd:PHA03307  342 SPgPSPSRSPSPSR---PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGR 406
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 30-61 2.39e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 2.39e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 971825946   30 YGGTALHAAALS-GHVSTVKLLLENNAQVDATD 61
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 3-134 2.67e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 47.70  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   3 AAGKGSDDVLRTMLsLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLEN-----NAQVDATDVMKHTPLFRACEMGHK 77
Cdd:cd22192   24 AAKENDVQAIKKLL-KCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVNQNL 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971825946  78 DVIQTLIKGGARVDLVDQDG-------HSLLHW-------AALGGNADVCQILIENKINPNVQDYAGRTPL 134
Cdd:cd22192  103 NLVRELIARGADVVSPRATGtffrpgpKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 80-150 3.23e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 3.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971825946  80 IQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLM 150
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02798 PHA02798
ankyrin-like protein; Provisional
 47-265 3.80e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  47 VKLLLENNAQVDATDVMKHTPLFRACEMGH---KDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNA---DVCQILIENK 120
Cdd:PHA02798  92 VKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKG 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 121 INPNV-QDYAGRTPLQCaaYGGY-INCMAV-----LMENNADPNIQDKEGRTALHWSCNNGYLDAIKL---LLDFA-AFP 189
Cdd:PHA02798 172 VDINThNNKEKYDTLHC--YFKYnIDRIDAdilklFVDNGFIINKENKSHKKKFMEYLNSLLYDNKRFkknILDFIfSYI 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 190 NQMENNEERYTPLDYALLGERHEVIQFMLEHGAlSIAAIQDIA------AFKIQAVYKGYKVRKAFRDRKNLLMKHEQLR 263
Cdd:PHA02798 250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGG-DINIITELGntclftAFENESKFIFNSILNKKPNKNTISYTYYKLR 328


                 ..
gi 971825946 264 KD 265
Cdd:PHA02798 329 KH 330
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 63-222 5.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 5.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  63 MKHTPLFRACEMGHKDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGY 142
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 143 INCMAVLMENNADPN-IQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQmeNNEERYTPLDYALLGERHEVIQFMLEHG 221
Cdd:PHA02875  81 VKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDI--PNTDKFSPLHLAVMMGDIKGIELLIDHK 158


                 .
gi 971825946 222 A 222
Cdd:PHA02875 159 A 159
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 3-151 8.97e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 8.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   3 AAGKGSDDVLRTMLslKSDIDINMADKYGGTALHAAALSGHVSTVKLLLENNAQVDAT---DVMKHTPLFRAC---EMGH 76
Cdd:PLN03192 629 AAKRNDLTAMKELL--KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAntdDDFSPTELRELLqkrELGH 706

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 971825946  77 KDVIqtlikggarVDLVDQDgHSLLHWAALGGNADVCQILIENKINPNVQDYAG----RTPLQCAAYGGYINCMAVLME 151
Cdd:PLN03192 707 SITI---------VDSVPAD-EPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGhpllRNERCCNEAGKLINLPPSLEE 775
Ank_5 pfam13857
Ankyrin repeats (many copies);
21-68 1.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 971825946   21 DIDINMADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPL 68
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 96-125 2.50e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 2.50e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 971825946    96 DGHSLLHWAALGGNADVCQILIENKINPNV 125
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 583-614 3.28e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 38.68  E-value: 3.28e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 971825946 583 RKELFRKKNKAAAVIQRAWRSYQLRKHLSHLR 614
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 96-127 3.57e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 3.57e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 971825946   96 DGHSLLHWAAL-GGNADVCQILIENKINPNVQD 127
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 130-161 4.34e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 4.34e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 971825946  130 GRTPLQCAAY-GGYINCMAVLMENNADPNIQDK 161
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 162-190 4.68e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 4.68e-04
                           10        20
                   ....*....|....*....|....*....
gi 971825946   162 EGRTALHWSCNNGYLDAIKLLLDFAAFPN 190
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-219 6.89e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.15  E-value: 6.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946    3 AAGKGSDDVLRTMLSLKSDIDINMADKYGGTALHAAALSG-HVSTVKLLLENNAQVDATDVMKHT---PLFRACEMGHKD 78
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAislEYVDAVEAILLH 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946   79 VIQTLIKGGARVDLVDQD------GHSLLHWAALGGNADVCQILIENKINPNV------------QDYA--GRTPLQCAA 138
Cdd:TIGR00870 104 LLAAFRKSGPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  139 YGGYINCMAVLMENNADPNIQDKEGRTALH-------WSCNNGYL-----DAIKLLLDFAAFPNQMEN--NEERYTPLDY 204
Cdd:TIGR00870 184 CLGSPSIVALLSEDPADILTADSLGNTLLHllvmeneFKAEYEELscqmyNFALSLLDKLRDSKELEVilNHQGLTPLKL 263

                         250
                  ....*....|....*
gi 971825946  205 ALLGERHEVIQFMLE 219
Cdd:TIGR00870 264 AAKEGRIVLFRLKLA 278
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 10-171 7.65e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 7.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  10 DVLRTMLSLKSDIDINMADKY--GGTALHAAALSGHVSTVKLLLENNAQVDAT---DVMKHTPL-----------FRACe 73
Cdd:cd21882   50 EAAPDSGNPKELVNAPCTDEFyqGQTALHIAIENRNLNLVRLLVENGADVSARatgRFFRKSPGnlfyfgelplsLAAC- 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  74 MGHKDVIQTLIKGGARV-DLVDQD--GHSLLHWAALGGN------ADVCQ-----ILIENKINPNVQ-----DYAGRTPL 134
Cdd:cd21882  129 TNQEEIVRLLLENGAQPaALEAQDslGNTVLHALVLQADntpensAFVCQmynllLSYGAHLDPTQQleeipNHQGLTPL 208

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 971825946 135 QCAAYGGYINCMAVLMENNADPNIQDKEgRTALHWSC 171
Cdd:cd21882  209 KLAAVEGKIVMFQHILQREFSGPYQPLS-RKFTEWTY 244
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 96-125 7.97e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 7.97e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 971825946   96 DGHSLLHWAALGGNADVCQILIENKINPNV 125
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 130-158 8.87e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 8.87e-04
                           10        20
                   ....*....|....*....|....*....
gi 971825946   130 GRTPLQCAAYGGYINCMAVLMENNADPNI 158
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 30-59 1.16e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 1.16e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 971825946   30 YGGTALHAAALSGHVSTVKLLLENNAQVDA 59
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 33-59 1.65e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 1.65e-03
                           10        20
                   ....*....|....*....|....*..
gi 971825946    33 TALHAAALSGHVSTVKLLLENNAQVDA 59
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 227-253 1.82e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 36.37  E-value: 1.82e-03
                         10        20
                 ....*....|....*....|....*..
gi 971825946 227 AIQDIAAFKIQAVYKGYKVRKAFRDRK 253
Cdd:cd23767    6 QRMNRAATLIQALWRGYKVRKELKKKK 32
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 79-255 2.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  79 VIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNI 158
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 159 QDkegrTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEEryTPLDYALLGER-HEVIQFMLEHGAlsiaaiqDIAAFKIQ 237
Cdd:PHA02876 240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKN--TPLHHASQAPSlSRLVPKLLERGA-------DVNAKNIK 306

                        170
                 ....*....|....*...
gi 971825946 238 AVYKGYKVRKAFRDRKNL 255
Cdd:PHA02876 307 GETPLYLMAKNGYDTENI 324
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 285-491 4.96e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  285 GRRSPDSCRPQALPCLPSTQDVPSRQSRAPSKQPPAGNVAQGPEPRDSRGSPGGSLGGALQKEQHVSSDLQGTNSRRPNE 364
Cdd:PHA03307   75 PGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPA 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  365 TAREHSKGQSACVHFRP-----NEGSDGSRHPGVPSVEK--SRGETAGDERCAKGKGFVKQPSCIRVAGPDEKGEDSRRA 437
Cdd:PHA03307  155 AGASPAAVASDAASSRQaalplSSPEETARAPSSPPAEPppSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGA 234

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 971825946  438 AAS----LPPHDSHWKP-SRRHDTEPKAKCAPQKRRTQELRGGRCSPAGSSRPGSARGE 491
Cdd:PHA03307  235 SSSdsssSESSGCGWGPeNECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRE 293
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 35-222 6.14e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 6.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  35 LHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRAC----EMGHKDVIQTLIK------------------------- 85
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKcsvfytlvaikdafnnrnveifkii 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  86 ------GGARVDLVDQDGHSLLHWAalggNADVCQILIENKINPNVQD-YAGRTPLQCAAYGGYINCMAVLMENNADPNI 158
Cdd:PHA02878 121 ltnrykNIQTIDLVYIDKKSKDDII----EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNI 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971825946 159 QDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMenNEERYTPLDYAL-LGERHEVIQFMLEHGA 222
Cdd:PHA02878 197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDAR--DKCGNTPLHISVgYCKDYDILKLLLEHGV 259
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 162-191 7.17e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 7.17e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 971825946  162 EGRTALHWSC-NNGYLDAIKLLLDFAAFPNQ 191
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
COG3416 COG3416
Uncharacterized conserved protein, DUF2076 domain [Function unknown];
260-345 7.20e-03

Uncharacterized conserved protein, DUF2076 domain [Function unknown];


Pssm-ID: 442642 [Multi-domain]  Cd Length: 237  Bit Score: 38.85  E-value: 7.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946 260 EQLRKDAAAKKREEENKRKEAEQQKGRRSP----------DSCRPQALPCLPSTQDVPSRQS----RAPSKQPPAGNVAQ 325
Cdd:COG3416   54 EAALKQAQQRIQELEAQLAQLQQQQPQSSGgflsglfgggQRPPPAPQPSQPGPQQQPAPPSgpwgQAAPQQPGYGQPQY 133

                         90       100
                 ....*....|....*....|.
gi 971825946 326 G-PEPRDSRGspGGSLGGALQ 345
Cdd:COG3416  134 GqPAAGPSGG--GGFLGGALQ 152
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 10-164 7.21e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 39.79  E-value: 7.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  10 DVLRTMLSLKSDIDINMADKY--GGTALHAAALSGHVSTVKLLLENNAQVDAT---DVMKHT-----------PLFRACE 73
Cdd:cd22196   71 DIAEKTGNLKEFVNAAYTDSYykGQTALHIAIERRNMHLVELLVQNGADVHARasgEFFKKKkggpgfyfgelPLSLAAC 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  74 MGHKDVIQTLIKG---GARVDLVDQDGHSLLHwaALGGNADVCQ------------ILIE-NKINPNVQ-----DYAGRT 132
Cdd:cd22196  151 TNQLDIVKFLLENphsPADISARDSMGNTVLH--ALVEVADNTPentkfvtkmyneILILgAKIRPLLKleeitNKKGLT 228

                        170       180       190
                 ....*....|....*....|....*....|..
gi 971825946 133 PLQCAAYGGYINCMAVLMENnadpNIQDKEGR 164
Cdd:cd22196  229 PLKLAAKTGKIGIFAYILGR----EIKEPECR 256
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 278-534 8.47e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.77  E-value: 8.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  278 KEAEQQKGRRSPDSCRPQALPCLPSTQDVPSRQSRAPSKQPPAGNVAQGPEPRDSRGSPGGSLGGALQKEQHVSSDLQGT 357
Cdd:PHA03307   95 LAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAAL 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  358 NSRRPNETAREHSKGQSACVHFRPNE-GSDGSRHPGVPSVEKSRGETAGDER--------------------CAKGK--- 413
Cdd:PHA03307  175 PLSSPEETARAPSSPPAEPPPSTPPAaASPRPPRRSSPISASASSPAPAPGRsaaddagasssdssssessgCGWGPene 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971825946  414 ------GFVKQPSCIRVA-GPDEKGEDSRRAAASLPPHDSHWKPSRRHDTEPKAKCAPQKRRTQELRGGRCSPAGSSRPG 486
Cdd:PHA03307  255 cplprpAPITLPTRIWEAsGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSE 334

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 971825946  487 SARGEAVHAGqnPPHHRTPRNKVTQAKLTGGLYSHLPQSTEELRSGAR 534
Cdd:PHA03307  335 SSRGAAVSPG--PSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAA 380
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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